P10795 (RBS1A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribulose bisphosphate carboxylase small chain 1A, chloroplastic
Short name=RuBisCO small subunit 1A
EC=4.1.1.39

Gene names

Name:	RBCS-1A
Synonyms:	ATS1A
Ordered Locus Names:	At1g67090
ORF Names:	F1O19.14, F5A8.1

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity.
Catalytic activity	2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.
Subunit structure	8 large chains + 8 small chains.
Subcellular location	Plastid › chloroplast membrane; Peripheral membrane protein. Plastid › chloroplast stroma Ref.6.
Miscellaneous	There are four genes coding for RBS in Arabidopsis thaliana.
Sequence similarities	Belongs to the RuBisCO small chain family.
Sequence caution	The sequence AAK49590.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA31948.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation Photorespiration Photosynthesis
Cellular component	Chloroplast Membrane Plastid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chloroplast ribulose bisphosphate carboxylase complex biogenesis Inferred from mutant phenotype PubMed 22223809. Source: TAIR photorespiration Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis Inferred from mutant phenotype PubMed 22223809. Source: TAIR reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW response to blue light Inferred from expression pattern PubMed 18820083. Source: TAIR response to cold Inferred from expression pattern PubMed 14535880. Source: TAIR response to far red light Inferred from expression pattern PubMed 18820083. Source: TAIR response to red light Inferred from expression pattern PubMed 18820083. Source: TAIR
Cellular_component	apoplast Inferred from direct assay PubMed 18538804. Source: TAIR chloroplast envelope Inferred from direct assay Ref.6PubMed 12938931PubMed 20061580. Source: TAIR chloroplast membrane Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast stroma Inferred from direct assay PubMed 16207701PubMed 18633119PubMed 20061580. Source: TAIR chloroplast thylakoid membrane Inferred from direct assay PubMed 15322131. Source: TAIR cytosolic ribosome Inferred from direct assay PubMed 15821981. Source: TAIR thylakoid lumen Inferred from direct assay PubMed 11719511. Source: TAIR
Molecular_function	copper ion binding Inferred from direct assay PubMed 16526091. Source: TAIR monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P10795-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 55	55	Chloroplast
	Chain	56 – 180	125	Ribulose bisphosphate carboxylase small chain 1A, chloroplastic		PRO_0000031463
Amino acid modifications
	Modified residue	79	1	Phosphoserine Ref.7
	Modified residue	113	1	Phosphoserine Ref.7
	Modified residue	177	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	115	1	G → R in AAG40356. Ref.4
	Sequence conflict	171	1	I → V in CAA31948. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 10, 2003. Version 2. Checksum: 5DE768676D61F8F7	FASTA	180	20,216
	10 20 30 40 50 60 MASSMLSSAT MVASPAQATM VAPFNGLKSS AAFPATRKAN NDITSITSNG GRVNCMQVWP 70 80 90 100 110 120 PIGKKKFETL SYLPDLTDSE LAKEVDYLIR NKWIPCVEFE LEHGFVYREH GNSPGYYDGR 130 140 150 160 170 180 YWTMWKLPLF GCTDSAQVLK EVEECKKEYP NAFIRIIGFD NTRQVQCISF IAYKPPSFTG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Four genes in two diverged subfamilies encode the ribulose-1,5-bisphosphate carboxylase small subunit polypeptides of Arabidopsis thaliana." Krebbers E., Seurinck J., Herdies L., Cashmore A.R., Timko M.P. Plant Mol. Biol. 11:745-759(1988) [AGRICOLA] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Columbia K85.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Arabidopsis thaliana small subunit leader and transit peptide enhance the expression of Bacillus thuringiensis proteins in transgenic plants." Wong E.Y., Hironaka C.M., Fishhoff D.A. Plant Mol. Biol. 20:81-93(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-79.
[6]	"Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana." Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N. Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: cv. Wassilewskija.
[7]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-113 AND SER-177, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X13611 Genomic DNA. Translation: CAA31948.1. Sequence problems. AC004146 Genomic DNA. Translation: AAD10655.1. AC007152 Genomic DNA. No translation available. CP002684 Genomic DNA. Translation: AEE34594.1. AF325011 mRNA. Translation: AAG40363.1. AF325004 mRNA. Translation: AAG40356.1. AF372874 mRNA. Translation: AAK49590.1. Different initiation. AF410291 mRNA. Translation: AAK95277.1. AY054188 mRNA. Translation: AAL06849.1. AY054581 mRNA. Translation: AAK96772.1. AY058831 mRNA. Translation: AAL24219.1. AY059940 mRNA. Translation: AAL24422.1. AY062612 mRNA. Translation: AAL32690.1. AY062711 mRNA. Translation: AAL32789.1. AY065101 mRNA. Translation: AAL38277.1. AY093380 mRNA. Translation: AAM13379.1. AY093388 mRNA. Translation: AAM13387.1. AY097366 mRNA. Translation: AAM19882.1. BT000362 mRNA. Translation: AAN15681.1. BT002076 mRNA. Translation: AAN72087.1. X68342 Other DNA. Translation: CAA48415.1. Different termination.
IPI	IPI00539020.
PIR	G96694. RKMUA1. S03720.
RefSeq	NP_176880.1. NM_105379.3.
UniGene	At.12721. At.30194. At.37531. At.46639. At.49098. At.67454. At.68122. At.70032. At.70053.
3D structure databases
ProteinModelPortal	P10795.
SMR	P10795. Positions 56-178.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10795. 4 interactions.
MINT	MINT-2584041.
2D gel databases
World-2DPAGE	0003:P10795.
Proteomic databases
PaxDb	P10795.
PRIDE	P10795.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G67090.1; AT1G67090.1; AT1G67090.
GeneID	843029.
KEGG	ath:AT1G67090.
Organism-specific databases
TAIR	At1g67090.
Phylogenomic databases
eggNOG	COG4451.
HOGENOM	HOG000141332.
InParanoid	P10795.
KO	K01602.
OMA	AFPATRK.
PhylomeDB	P10795.
ProtClustDB	PLN02289.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G67090-MONOMER.
Gene expression databases
Genevestigator	P10795.
Family and domain databases
Gene3D	3.30.190.10. 1 hit.
InterPro	IPR024681. RuBisCO_sc. IPR000894. RuBisCO_sc_dom. IPR024680. RuBisCO_ssu_N. [Graphical view]
Pfam	PF12338. RbcS. 1 hit. PF00101. RuBisCO_small. 1 hit. [Graphical view]
PRINTS	PR00152. RUBISCOSMALL.
SMART	SM00961. RuBisCO_small. 1 hit. [Graphical view]
SUPFAM	SSF55239. RuBisCO_small. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RBS1A_ARATH

Accession

Primary (citable) accession number: P10795
Secondary accession number(s): Q94JW2, Q9FPI6, Q9SAV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 10, 2003
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program